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Calcium in PDB 2e81: Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine

Enzymatic activity of Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine

All present enzymatic activity of Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine:
1.7.2.2;

Protein crystallography data

The structure of Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine, PDB code: 2e81 was solved by O.Einsle, P.M.H.Kroneck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 119.891, 119.891, 186.224, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.3

Other elements in 2e81:

The structure of Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine also contains other interesting chemical elements:

Iron (Fe) 5 atoms
Yttrium (Y) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine (pdb code 2e81). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine, PDB code: 2e81:

Calcium binding site 1 out of 1 in 2e81

Go back to Calcium Binding Sites List in 2e81
Calcium binding site 1 out of 1 in the Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Cytochrome C Nitrite Reductase From Wolinella Succinogenes with Bound Intermediate Hydroxylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca513

b:42.3
occ:1.00
 O A:LYS274 2.4 31.1 1.0
OE1 A:GLN276 2.4 40.9 1.0
O A:HOH1610 2.4 30.1 1.0
O A:HOH1740 2.5 36.3 1.0
OE2 A:GLU217 2.5 31.8 1.0
O A:TYR218 2.5 32.2 1.0
OE1 A:GLU217 2.7 29.0 1.0
CD A:GLU217 2.9 34.1 1.0
C A:LYS274 3.6 29.7 1.0
CD A:GLN276 3.6 40.7 1.0
C A:TYR218 3.7 33.8 1.0
OH A:TYR255 3.7 27.9 1.0
OD2 A:ASP262 4.1 31.9 1.0
N A:TYR218 4.2 30.2 1.0
N A:GLN276 4.3 27.3 1.0
NE2 A:GLN276 4.3 38.7 1.0
CA A:ALA275 4.3 28.6 1.0
CG A:GLU217 4.4 32.8 1.0
N A:ALA275 4.4 28.9 1.0
CA A:LYS274 4.5 29.4 1.0
CZ A:TYR255 4.5 32.4 1.0
CB A:TYR219 4.5 33.5 1.0
N A:TYR219 4.6 32.2 1.0
CA A:TYR218 4.6 31.7 1.0
C A:ALA275 4.6 29.3 1.0
CA A:TYR219 4.6 33.5 1.0
CZ3 A:TRP391 4.6 26.2 1.0
CB A:LYS274 4.6 25.5 1.0
N A:LYS274 4.7 27.6 1.0
OD1 A:ASP262 4.7 33.7 1.0
CG A:GLN276 4.7 32.4 1.0
CG A:ASP262 4.8 33.4 1.0
CB A:GLN276 4.8 27.7 1.0
O A:HOH1722 4.9 42.1 1.0
CH2 A:TRP391 4.9 26.7 1.0
CE2 A:TYR255 5.0 29.1 1.0

Reference:

O.Einsle, A.Messerschmidt, R.Huber, P.M.H.Kroneck, F.Neese. Mechanism of the Six-Electron Reduction of Nitrite to Ammonia By Cytochrome C Nitrite Reductase J.Am.Chem.Soc. V. 124 11737 2002.
ISSN: ISSN 0002-7863
PubMed: 12296741
DOI: 10.1021/JA0206487
Page generated: Fri Jul 12 10:07:28 2024

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